Domains of phenylalanyl-tRNA synthetase from Thermus thermophilus required for aminoacylation.
The contribution of entire domains or particular amino acid residues of the phenylalanyl-tRNA synthetase (FRS) from Thermus thermophilus to the interaction with tRNA(Phe) was studied. Removal of domain 8 of the beta subunit resulted in drastic reduction of the dissociation constant of the FRS x tRNA(Phe) complex. Neither the removal of arginine 2 of the beta subunit, which makes the only major contact between domains beta1-5 and the tRNA, nor the replacement of the conserved proline 473 by glycine had an influence on the aminoacylation activity of the FRS. Thus, the body comprising domains 1-5 of the beta subunit may not be essential for efficient aminoacylation of tRNA(Phe) by the FRS and rather be involved in other functions.
Lechler
A
A
Laboratorium für Biochemie, Universität Bayreuth, Germany.
Kreutzer
R
R
D000215:Acylation; D000255:Adenosine Triphosphate / Q000378:metabolism; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D016296:Mutagenesis / Q000235:genetics; D010652:Phenylalanine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D017384:Sequence Deletion / Q000235:genetics; D013696:Temperature; D016963:Thermus thermophilus / Q000201:enzymology*
D012346:RNA, Transfer, Amino Acyl; D000255:Adenosine Triphosphate; D010652:Phenylalanine-tRNA Ligase